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WRKY group IId transcription factors interact with calmodulin
Author(s) -
Park Chan Young,
Lee Ju Huck,
Yoo Jae Hyuk,
Moon Byeong Cheol,
Choi Man Soo,
Kang Yun Hwan,
Lee Sang Min,
Kim Ho Soo,
Kang Kyu Young,
Chung Woo Sik,
Lim Chae Oh,
Cho Moo Je
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.01.057
Subject(s) - calmodulin , wrky protein domain , transcription factor , arabidopsis , complementary dna , horseradish peroxidase , biology , cdna library , binding site , signal transducing adaptor protein , binding protein , microbiology and biotechnology , biochemistry , chemistry , enzyme , signal transduction , gene , mutant
Calmodulin (CaM) is a ubiquitous Ca 2+ ‐binding protein known to regulate diverse cellular functions by modulating the activity of various target proteins. We isolated a cDNA encoding AtWRKY7, a novel CaM‐binding transcription factor, from an Arabidopsis expression library with horseradish peroxidase‐conjugated CaM. CaM binds specifically to the Ca 2+ ‐dependent CaM‐binding domain (CaMBD) of AtWRKY7, as shown by site‐directed mutagenesis, a gel mobility shift assay, a split‐ubiquitin assay, and a competition assay using a Ca 2+ /CaM‐dependent enzyme. Furthermore, we show that the CaMBD of AtWRKY7 is a conserved structural motif (C‐motif) found in group IId of the WRKY protein family.